BMC domain

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BMC
PDB 2a1b EBI.jpg
carboxysome shell protein ccmk2
Identifiers
Symbol BMC
Pfam PF00936
InterPro IPR000249
PROSITE PDOC00876

In molecular biology the Bacterial Microcompartment (BMC) domain is a protein domain found in a variety of shell proteins, including CsoS1A, CsoS1B and CsoS1C of Thiobacillus neapolitanus (Halothiobacillus neapolitanus) and their orthologs from other bacteria. These shell proteins form the polyhedral structure of the carboxysome and related structures that plays a metabolic role in bacteria. The BMC domain consists of about 90 amino acid residues, characterized by β-α-β motif connected by a β-hairpin.

The majority of the shell proteins consist of a single BMC domain in each subunit, forming a hexameric structure that assembles to form the flat facets of the polyhedral shell.[1] To date, two shell proteins were found to consist a tandem BMC domains, of which forms a trimeric structure, giving a pseudo-hexameric appearance.[2][3]

References[edit]

  1. ^ Kerfeld, C. A.; Sawaya, M. R.; Tanaka, S.; Nguyen, C. V.; Phillips, M.; Beeby, M.; Yeates, T. O. (2005). "Protein Structures Forming the Shell of Primitive Bacterial Organelles". Science 309 (5736): 936–938. doi:10.1126/science.1113397. PMID 16081736.  edit
  2. ^ Heldt, D.; Frank, S.; Seyedarabi, A.; Ladikis, D.; Parsons, J. B.; Warren, M. J.; Pickersgill, R. W. (2009). "Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization inClostridium kluyveri". Biochemical Journal 423 (2): 199–207. doi:10.1042/BJ20090780. PMID 19635047.  edit
  3. ^ Pang, A.; Warren, M. J.; Pickersgill, R. W. (2011). "Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe–4S cluster-binding site". Acta Crystallographica Section D Biological Crystallography 67 (2): 91–96. doi:10.1107/S0907444910050201. PMID 21245529.  edit

This article incorporates text from the public domain Pfam and InterPro IPR000249